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Nucleic Acids Research Advance Access originally published online on October 24, 2007
Nucleic Acids Research 2007 35(20):e137; doi:10.1093/nar/gkm818
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Nucleic Acids Research, 2007, Vol. 35, No. 20 e137
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Methods Online

A comprehensive set of plasmids for vanillate- and xylose-inducible gene expression in Caulobacter crescentus

Martin Thanbichler1,*, Antonio A. Iniesta2 and Lucy Shapiro2

1Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch-Straße, 35043 Marburg, Germany and 2Department of Developmental Biology, Stanford University School of Medicine, Beckman Center B300, 279 Campus Drive, Stanford, CA 94305, USA

*To whom correspondence should be addressed. Tel: +49 6421 178330, Fax: +49 6421 178209; Email: thanbichler{at}mpi-marburg.mpg.de

Received August 24, 2007. Revised September 17, 2007. Accepted September 18, 2007.

Caulobacter crescentus is widely used as a powerful model system for the study of prokaryotic cell biology and development. Analysis of this organism is complicated by a limited selection of tools for genetic manipulation and inducible gene expression. This study reports the identification and functional characterization of a vanillate-regulated promoter (Pvan) which meets all requirements for application as a multi-purpose expression system in Caulobacter, thus complementing the established xylose-inducible system (Pxyl). Furthermore, we introduce a newly constructed set of integrating and replicating shuttle vectors that considerably facilitate cell biological and physiological studies in Caulobacter. Based on different narrow and broad-host range replicons, they offer a wide choice of promoters, resistance genes, and fusion partners for the construction of fluorescently or affinity-tagged proteins. Since many of these constructs are also suitable for use in other bacteria, this work provides a comprehensive collection of tools that will enrich many areas of microbiological research.


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[Abstract] [Full Text] [PDF]


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